PRE3/YJL001W Literature Guide Help

Other names published for PRE3: CRL21, proteasome core particle subunit beta 1, YJL001W

PRE3 - Additional Literature (82)

ReferenceOther Genes Addressed
Breker M, et al.  (2013) A novel single-cell screening platform reveals proteome plasticity during yeast stress responses. J Cell Biol 200(6):839-50
Peth A, et al.  (2013) Ubiquitinated proteins activate the proteasomal ATPases by binding to usp14 or uch37 homologs. J Biol Chem 288(11):7781-90
Beck F, et al.  (2012) Near-atomic resolution structural model of the yeast 26S proteasome. Proc Natl Acad Sci U S A 109(37):14870-5
Dengjel J, et al.  (2012) Identification of autophagosome-associated proteins and regulators by quantitative proteomic analysis and genetic screens. Mol Cell Proteomics 11(3):M111.014035
Enenkel C  (2012) Using Native Gel Electrophoresis and Phosphofluoroimaging to Analyze GFP-Tagged Proteasomes. Methods Mol Biol 832():339-48
Gallastegui N and Groll M  (2012) Analysing properties of proteasome inhibitors using kinetic and x-ray crystallographic studies. Methods Mol Biol 832():373-90
Ha SW, et al.  (2012) The N-terminal domain of Rpn4 serves as a portable ubiquitin-independent degron and is recognized by specific 19S RP subunits. Biochem Biophys Res Commun 419(2):226-31
Hodgins-Davis A, et al.  (2012) Abundant gene-by-environment interactions in gene expression reaction norms to copper within Saccharomyces cerevisiae. Genome Biol Evol 4(11):1061-79
Jacobson T, et al.  (2012) Arsenite interferes with protein folding and triggers formation of protein aggregates in yeast. J Cell Sci 125(Pt 21):5073-83
Kimura A, et al.  (2012) N-myristoylation of the Rpt2 subunit regulates intracellular localization of the yeast 26S proteasome. Biochemistry 51(44):8856-66
Takagi K, et al.  (2012) Structural basis for specific recognition of Rpt1p, an ATPase subunit of 26 S proteasome, by proteasome-dedicated chaperone Hsm3p. J Biol Chem 287(15):12172-82
Tallec BL and Peyroche A  (2012) Using DNA damage sensitivity phenotypes to characterize mutations affecting proteasome function. Methods Mol Biol 832():363-71
Bonzanni N, et al.  (2011) The role of proteosome-mediated proteolysis in modulating potentially harmful transcription factor activity in Saccharomyces cerevisiae. Bioinformatics 27(13):i283-i287
Couttas TA, et al.  (2011) Monitoring cytoplasmic protein complexes with blue native gel electrophoresis and stable isotope labelling with amino acids in cell culture: analysis of changes in the 20S proteasome. Electrophoresis 32(14):1819-23
Gaczynska M and Osmulski PA  (2011) Atomic force microscopy of proteasome assemblies. Methods Mol Biol 736():117-32
Gandhi SJ, et al.  (2011) Transcription of functionally related constitutive genes is not coordinated. Nat Struct Mol Biol 18(1):27-34
Gomez TA, et al.  (2011) Identification of a functional docking site in the Rpn1 LRR domain for the UBA-UBL domain protein Ddi1. BMC Biol 9(1):33
Henderson A, et al.  (2011) Dependence of proteasome processing rate on substrate unfolding. J Biol Chem 286(20):17495-502
Kraut DA and Matouschek A  (2011) Proteasomal degradation from internal sites favors partial proteolysis via remote domain stabilization. ACS Chem Biol 6(10):1087-95
Sakata E, et al.  (2011) The catalytic activity of Ubp6 enhances maturation of the proteasomal regulatory particle. Mol Cell 42(5):637-49
da Cunha FM, et al.  (2011) Aging and calorie restriction modulate yeast redox state, oxidized protein removal, and the ubiquitin-proteasome system. Free Radic Biol Med 51(3):664-70
Archer CT and Kodadek T  (2010) The hydrophobic patch of ubiquitin is required to protect transactivator-promoter complexes from destabilization by the proteasomal ATPases. Nucleic Acids Res 38(3):789-96
Chandra A, et al.  (2010) Synthetic lethality of rpn11-1 rpn10Delta is linked to altered proteasome assembly and activity. Curr Genet 56(6):543-57
Grassl J, et al.  (2010) Analysis of the budding yeast pH 4-7 proteome in meiosis. Proteomics 10(3):506-19
Kikuchi J, et al.  (2010) Co- and post-translational modifications of the 26S proteasome in yeast. Proteomics 10(15):2769-79
Lionnet T, et al.  (2010) Nuclear physics: quantitative single-cell approaches to nuclear organization and gene expression. Cold Spring Harb Symp Quant Biol 75():113-26
Sadre-Bazzaz K, et al.  (2010) Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening. Mol Cell 37(5):728-35
Stadtmueller BM, et al.  (2010) Structural models for interactions between the 20S proteasome and its PAN/19S activators. J Biol Chem 285(1):13-7
Voloshin O, et al.  (2010) Tubulin chaperone E binds microtubules and proteasomes and protects against misfolded protein stress. Cell Mol Life Sci 67(12):2025-38
Wakata A, et al.  (2010) Simultaneous fluorescent monitoring of proteasomal subunit catalysis. J Am Chem Soc 132(5):1578-82